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Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase

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Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase. / Goncalves, Victor; Brannigan, James A.; Laporte, Alice; Bell, Andrew S.; Roberts, Shirley M.; Wilkinson, Anthony J.; Leatherbarrow, Robin J.; Tate, Edward W.

In: MedChemComm, Vol. 8, No. 1, 2017, p. 191-197.

Research output: Contribution to journalArticle

Harvard

Goncalves, V, Brannigan, JA, Laporte, A, Bell, AS, Roberts, SM, Wilkinson, AJ, Leatherbarrow, RJ & Tate, EW 2017, 'Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase', MedChemComm, vol. 8, no. 1, pp. 191-197. https://doi.org/10.1039/c6md00531d

APA

Goncalves, V., Brannigan, J. A., Laporte, A., Bell, A. S., Roberts, S. M., Wilkinson, A. J., ... Tate, E. W. (2017). Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase. MedChemComm, 8(1), 191-197. https://doi.org/10.1039/c6md00531d

Vancouver

Goncalves V, Brannigan JA, Laporte A, Bell AS, Roberts SM, Wilkinson AJ et al. Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase. MedChemComm. 2017;8(1):191-197. https://doi.org/10.1039/c6md00531d

Author

Goncalves, Victor ; Brannigan, James A. ; Laporte, Alice ; Bell, Andrew S. ; Roberts, Shirley M. ; Wilkinson, Anthony J. ; Leatherbarrow, Robin J. ; Tate, Edward W. / Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase. In: MedChemComm. 2017 ; Vol. 8, No. 1. pp. 191-197.

Bibtex - Download

@article{52753508a7e5465c889285358cbc2328,
title = "Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase",
abstract = "The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falciparum N-myristoyltransferase (NMT).",
author = "Victor Goncalves and Brannigan, {James A.} and Alice Laporte and Bell, {Andrew S.} and Roberts, {Shirley M.} and Wilkinson, {Anthony J.} and Leatherbarrow, {Robin J.} and Tate, {Edward W.}",
note = "{\circledC} 2017, The Royal Society of Chemistry.",
year = "2017",
doi = "10.1039/c6md00531d",
language = "English",
volume = "8",
pages = "191--197",
journal = "MedChemComm",
issn = "2040-2503",
publisher = "Royal Society of Chemistry",
number = "1",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase

AU - Goncalves, Victor

AU - Brannigan, James A.

AU - Laporte, Alice

AU - Bell, Andrew S.

AU - Roberts, Shirley M.

AU - Wilkinson, Anthony J.

AU - Leatherbarrow, Robin J.

AU - Tate, Edward W.

N1 - © 2017, The Royal Society of Chemistry.

PY - 2017

Y1 - 2017

N2 - The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falciparum N-myristoyltransferase (NMT).

AB - The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falciparum N-myristoyltransferase (NMT).

UR - http://www.scopus.com/inward/record.url?scp=85010749568&partnerID=8YFLogxK

U2 - 10.1039/c6md00531d

DO - 10.1039/c6md00531d

M3 - Article

VL - 8

SP - 191

EP - 197

JO - MedChemComm

JF - MedChemComm

SN - 2040-2503

IS - 1

ER -